3r0t - Revision history

OCA at 12:05, 14 March 2024

2024-03-14T12:05:40Z

←Older revision		Revision as of 12:05, 14 March 2024
Line 3:		Line 3:
	<StructureSection load='3r0t' size='340' side='right'caption='[[3r0t]], [[Resolution\|resolution]] 1.75Å' scene=''>		<StructureSection load='3r0t' size='340' side='right'caption='[[3r0t]], [[Resolution\|resolution]] 1.75Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[3r0t]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/~~Human Human~~]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3R0T OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3R0T FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[3r0t]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3R0T OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3R0T FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=FU9:3-(CYCLOPROPYLAMINO)-5-{[3-(TRIFLUOROMETHYL)PHENYL]AMINO}PYRIMIDO[4,5-C]QUINOLINE-8-CARBOXYLIC+ACID'>FU9</scene>, <scene name='pdbligand=PEG:DI(HYDROXYETHYL)ETHER'>PEG</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene~~></td></tr>~~	+	</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models\|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution\|Resolution]] 1.75Å</td></tr>
-	~~<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[3pe1\|3pe1]], [[3pe2\|3pe2]]</div></td></tr>~~	+	<tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=FU9:3-(CYCLOPROPYLAMINO)-5-{[3-(TRIFLUOROMETHYL)PHENYL]AMINO}PYRIMIDO[4,5-C]QUINOLINE-8-CARBOXYLIC+ACID'>FU9</scene>, <scene name='pdbligand=PEG:DI(HYDROXYETHYL)ETHER'>PEG</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
-	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">CSNK2A1, CK2A1 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>	+
-	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Non-specific_serine/threonine_protein_kinase Non-specific serine/threonine protein kinase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.11.1 2.7.11.1] </span></td></tr>	+
	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3r0t FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3r0t OCA], [https://pdbe.org/3r0t PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3r0t RCSB], [https://www.ebi.ac.uk/pdbsum/3r0t PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3r0t ProSAT]</span></td></tr>		<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3r0t FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3r0t OCA], [https://pdbe.org/3r0t PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3r0t RCSB], [https://www.ebi.ac.uk/pdbsum/3r0t PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3r0t ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
-	[[https://www.uniprot.org/uniprot/CSK21_HUMAN CSK21_HUMAN]] Catalytic subunit of a constitutively active serine/threonine-protein kinase complex that phosphorylates a large number of substrates containing acidic residues C-terminal to the phosphorylated serine or threonine. Regulates numerous cellular processes, such as cell cycle progression, apoptosis and transcription, as well as viral infection. May act as a regulatory node which integrates and coordinates numerous signals leading to an appropriate cellular response. During mitosis, functions as a component of the p53/TP53-dependent spindle assembly checkpoint (SAC) that maintains cyclin-B-CDK1 activity and G2 arrest in response to spindle damage. Also required for p53/TP53-mediated apoptosis, phosphorylating 'Ser-392' of p53/TP53 following UV irradiation. Can also negatively regulate apoptosis. Phosphorylates the caspases CASP9 and CASP2 and the apoptotic regulator NOL3. Phosphorylation protects CASP9 from cleavage and activation by CASP8, and inhibits the dimerization of CASP2 and activation of CASP8. Regulates transcription by direct phosphorylation of RNA polymerases I, II, III and IV. Also phosphorylates and regulates numerous transcription factors including NF-kappa-B, STAT1, CREB1, IRF1, IRF2, ATF1, SRF, MAX, JUN, FOS, MYC and MYB. Phosphorylates Hsp90 and its co-chaperones FKBP4 and CDC37, which is essential for chaperone function. Regulates Wnt signaling by phosphorylating CTNNB1 and the transcription factor LEF1. Acts as an ectokinase that phosphorylates several extracellular proteins. During viral infection, phosphorylates various proteins involved in the viral life cycles of EBV, HSV, HBV, HCV, HIV, CMV and HPV.<ref>PMID:11239457</ref> <ref>PMID:11704824</ref> <ref>PMID:16193064</ref> <ref>PMID:19188443</ref>	+	[https://www.uniprot.org/uniprot/CSK21_HUMAN CSK21_HUMAN] Catalytic subunit of a constitutively active serine/threonine-protein kinase complex that phosphorylates a large number of substrates containing acidic residues C-terminal to the phosphorylated serine or threonine. Regulates numerous cellular processes, such as cell cycle progression, apoptosis and transcription, as well as viral infection. May act as a regulatory node which integrates and coordinates numerous signals leading to an appropriate cellular response. During mitosis, functions as a component of the p53/TP53-dependent spindle assembly checkpoint (SAC) that maintains cyclin-B-CDK1 activity and G2 arrest in response to spindle damage. Also required for p53/TP53-mediated apoptosis, phosphorylating 'Ser-392' of p53/TP53 following UV irradiation. Can also negatively regulate apoptosis. Phosphorylates the caspases CASP9 and CASP2 and the apoptotic regulator NOL3. Phosphorylation protects CASP9 from cleavage and activation by CASP8, and inhibits the dimerization of CASP2 and activation of CASP8. Regulates transcription by direct phosphorylation of RNA polymerases I, II, III and IV. Also phosphorylates and regulates numerous transcription factors including NF-kappa-B, STAT1, CREB1, IRF1, IRF2, ATF1, SRF, MAX, JUN, FOS, MYC and MYB. Phosphorylates Hsp90 and its co-chaperones FKBP4 and CDC37, which is essential for chaperone function. Regulates Wnt signaling by phosphorylating CTNNB1 and the transcription factor LEF1. Acts as an ectokinase that phosphorylates several extracellular proteins. During viral infection, phosphorylates various proteins involved in the viral life cycles of EBV, HSV, HBV, HCV, HIV, CMV and HPV.<ref>PMID:11239457</ref> <ref>PMID:11704824</ref> <ref>PMID:16193064</ref> <ref>PMID:19188443</ref>
-	~~<div style="background-color:#fffaf0;">~~	+
-	~~== Publication Abstract from PubMed ==~~	+
-	5-(3-chlorophenylamino)benzo[c][2,6] naphthyridine-8 carboxylic acid (CX-4945), the first clinical stage inhibitor of protein kinase CK2 for the treatment of cancer, is representative of a new class of CK2 inhibitors with Ki values in the low nanomolar range and unprecedented selectivity versus other kinases. Here we present the crystal structure of the complexes between CX-4945 and two analogs (CX-5011 and CX-5279) with the catalytic subunit of human CK2. Consistent with their ATP competitive mode of inhibition, all three compounds bind in the active site of CK2 (Type I inhibitors). The tricyclic scaffold of the inhibitors superposes to the adenine of ATP establishing multiple hydrophobic interactions with the binding cavity. The more extended scaffold, as compared to that of ATP, allows the carboxylic function, shared by all three ligands, to penetrate into the deepest part of the active site where it makes interactions with conserved water W1 and Lys-68, thus accounting for the crucial role of this negatively charged group in conferring high potency to this class of inhibitors. The presence of a pyrimidine in CX-5011 and in CX-5279 instead of a pyridine (as in CX-4945) ring is likely to account for the higher specificity of these compounds whose Gini coefficients, calculated by profiling them against panels of 102 and/or 235 kinases, are significantly higher than that of CX-4945 (0.735 and 0.755 respectively, vs 0.615), denoting the highest selectivity ever reported for CK2 inhibitors.	+
-		+
-	Unprecedented selectivity and structural determinants of a new class of protein kinase CK2 inhibitors in clinical stage for the treatment of cancer.,Battistutta R, Cozza G, Pierre F, Papinutto E, Lolli G, Sarno S, O'Brien SE, Siddiqui-Jain A, Haddach M, Anderes K, Ryckman DM, Meggio F, Pinna LA Biochemistry. 2011 Aug 26. PMID:21870818<ref>PMID:21870818</ref>	+
-		+
-	~~From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>~~	+
-	~~</div>~~	+
-	~~<div class="pdbe-citations 3r0t" style="background-color:#fffaf0;"></div~~>	+

	==See Also==		==See Also==
Line 28:		Line 17:
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: ~~Human~~]]	+	[[Category: Homo sapiens]]
	[[Category: Large Structures]]		[[Category: Large Structures]]
-	~~[[Category: Non-specific serine/threonine protein kinase]]~~	+	[[Category: Battistutta R]]
-	[[Category: Battistutta, R]]	+	[[Category: Haddach M]]
-	[[Category: Haddach, M]]	+	[[Category: Lolli G]]
-	[[Category: Lolli, G]]	+	[[Category: Papinutto E]]
-	[[Category: Papinutto, E]]	+	[[Category: Pierre F]]
-	[[Category: Pierre, F]]	+	[[Category: Ryckman DM]]
-	[[Category: Ryckman~~, D M]]~~	+
-	~~[[Category: Ck2-inhibitor complex]]~~	+
-	~~[[Category: Kinase]]~~	+
-	~~[[Category: Transferase-transferase inhibitor complex~~]]	+

OCA at 05:44, 15 June 2022

2022-06-15T05:44:14Z

←Older revision		Revision as of 05:44, 15 June 2022
Line 1:		Line 1:

	==Crystal structure of human protein kinase CK2 alpha subunit in complex with the inhibitor CX-5279==		==Crystal structure of human protein kinase CK2 alpha subunit in complex with the inhibitor CX-5279==
-	<StructureSection load='3r0t' size='340' side='right' caption='[[3r0t]], [[Resolution\|resolution]] 1.75Å' scene=''>	+	<StructureSection load='3r0t' size='340' side='right'caption='[[3r0t]], [[Resolution\|resolution]] 1.75Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[3r0t]] is a 1 chain structure with sequence from [~~http~~://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3R0T OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=3R0T FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[3r0t]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3R0T OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3R0T FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=FU9:3-(CYCLOPROPYLAMINO)-5-{[3-(TRIFLUOROMETHYL)PHENYL]AMINO}PYRIMIDO[4,5-C]QUINOLINE-8-CARBOXYLIC+ACID'>FU9</scene>, <scene name='pdbligand=PEG:DI(HYDROXYETHYL)ETHER'>PEG</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>	+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=FU9:3-(CYCLOPROPYLAMINO)-5-{[3-(TRIFLUOROMETHYL)PHENYL]AMINO}PYRIMIDO[4,5-C]QUINOLINE-8-CARBOXYLIC+ACID'>FU9</scene>, <scene name='pdbligand=PEG:DI(HYDROXYETHYL)ETHER'>PEG</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
-	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[3pe1\|3pe1]], [[3pe2\|3pe2]]</td></tr>	+	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[3pe1\|3pe1]], [[3pe2\|3pe2]]</div></td></tr>
-	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">CSNK2A1, CK2A1 ([~~http~~://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>	+	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">CSNK2A1, CK2A1 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>
-	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[~~http~~://en.wikipedia.org/wiki/Non-specific_serine/threonine_protein_kinase Non-specific serine/threonine protein kinase], with EC number [~~http~~://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.11.1 2.7.11.1] </span></td></tr>	+	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Non-specific_serine/threonine_protein_kinase Non-specific serine/threonine protein kinase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.11.1 2.7.11.1] </span></td></tr>
-	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=3r0t FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3r0t OCA], [~~http~~://pdbe.org/3r0t PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=3r0t RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/3r0t PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=3r0t ProSAT]</span></td></tr>	+	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3r0t FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3r0t OCA], [https://pdbe.org/3r0t PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3r0t RCSB], [https://www.ebi.ac.uk/pdbsum/3r0t PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3r0t ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
-	[[~~http~~://www.uniprot.org/uniprot/CSK21_HUMAN CSK21_HUMAN]] Catalytic subunit of a constitutively active serine/threonine-protein kinase complex that phosphorylates a large number of substrates containing acidic residues C-terminal to the phosphorylated serine or threonine. Regulates numerous cellular processes, such as cell cycle progression, apoptosis and transcription, as well as viral infection. May act as a regulatory node which integrates and coordinates numerous signals leading to an appropriate cellular response. During mitosis, functions as a component of the p53/TP53-dependent spindle assembly checkpoint (SAC) that maintains cyclin-B-CDK1 activity and G2 arrest in response to spindle damage. Also required for p53/TP53-mediated apoptosis, phosphorylating 'Ser-392' of p53/TP53 following UV irradiation. Can also negatively regulate apoptosis. Phosphorylates the caspases CASP9 and CASP2 and the apoptotic regulator NOL3. Phosphorylation protects CASP9 from cleavage and activation by CASP8, and inhibits the dimerization of CASP2 and activation of CASP8. Regulates transcription by direct phosphorylation of RNA polymerases I, II, III and IV. Also phosphorylates and regulates numerous transcription factors including NF-kappa-B, STAT1, CREB1, IRF1, IRF2, ATF1, SRF, MAX, JUN, FOS, MYC and MYB. Phosphorylates Hsp90 and its co-chaperones FKBP4 and CDC37, which is essential for chaperone function. Regulates Wnt signaling by phosphorylating CTNNB1 and the transcription factor LEF1. Acts as an ectokinase that phosphorylates several extracellular proteins. During viral infection, phosphorylates various proteins involved in the viral life cycles of EBV, HSV, HBV, HCV, HIV, CMV and HPV.<ref>PMID:11239457</ref> <ref>PMID:11704824</ref> <ref>PMID:16193064</ref> <ref>PMID:19188443</ref>	+	[[https://www.uniprot.org/uniprot/CSK21_HUMAN CSK21_HUMAN]] Catalytic subunit of a constitutively active serine/threonine-protein kinase complex that phosphorylates a large number of substrates containing acidic residues C-terminal to the phosphorylated serine or threonine. Regulates numerous cellular processes, such as cell cycle progression, apoptosis and transcription, as well as viral infection. May act as a regulatory node which integrates and coordinates numerous signals leading to an appropriate cellular response. During mitosis, functions as a component of the p53/TP53-dependent spindle assembly checkpoint (SAC) that maintains cyclin-B-CDK1 activity and G2 arrest in response to spindle damage. Also required for p53/TP53-mediated apoptosis, phosphorylating 'Ser-392' of p53/TP53 following UV irradiation. Can also negatively regulate apoptosis. Phosphorylates the caspases CASP9 and CASP2 and the apoptotic regulator NOL3. Phosphorylation protects CASP9 from cleavage and activation by CASP8, and inhibits the dimerization of CASP2 and activation of CASP8. Regulates transcription by direct phosphorylation of RNA polymerases I, II, III and IV. Also phosphorylates and regulates numerous transcription factors including NF-kappa-B, STAT1, CREB1, IRF1, IRF2, ATF1, SRF, MAX, JUN, FOS, MYC and MYB. Phosphorylates Hsp90 and its co-chaperones FKBP4 and CDC37, which is essential for chaperone function. Regulates Wnt signaling by phosphorylating CTNNB1 and the transcription factor LEF1. Acts as an ectokinase that phosphorylates several extracellular proteins. During viral infection, phosphorylates various proteins involved in the viral life cycles of EBV, HSV, HBV, HCV, HIV, CMV and HPV.<ref>PMID:11239457</ref> <ref>PMID:11704824</ref> <ref>PMID:16193064</ref> <ref>PMID:19188443</ref>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
	== Publication Abstract from PubMed ==		== Publication Abstract from PubMed ==
Line 23:		Line 23:

	==See Also==		==See Also==
-	*[[Casein kinase\|Casein kinase]]	+	*[[Casein kinase 3D structures\|Casein kinase 3D structures]]
	== References ==		== References ==
	<references/>		<references/>
Line 29:		Line 29:
	</StructureSection>		</StructureSection>
	[[Category: Human]]		[[Category: Human]]
		+	[[Category: Large Structures]]
	[[Category: Non-specific serine/threonine protein kinase]]		[[Category: Non-specific serine/threonine protein kinase]]
	[[Category: Battistutta, R]]		[[Category: Battistutta, R]]

OCA at 10:48, 5 August 2016

2016-08-05T10:48:11Z

←Older revision		Revision as of 10:48, 5 August 2016
Line 1:		Line 1:
		+
	==Crystal structure of human protein kinase CK2 alpha subunit in complex with the inhibitor CX-5279==		==Crystal structure of human protein kinase CK2 alpha subunit in complex with the inhibitor CX-5279==
	<StructureSection load='3r0t' size='340' side='right' caption='[[3r0t]], [[Resolution\|resolution]] 1.75Å' scene=''>		<StructureSection load='3r0t' size='340' side='right' caption='[[3r0t]], [[Resolution\|resolution]] 1.75Å' scene=''>
Line 7:		Line 8:
	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">CSNK2A1, CK2A1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>		<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">CSNK2A1, CK2A1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>
	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Non-specific_serine/threonine_protein_kinase Non-specific serine/threonine protein kinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.11.1 2.7.11.1] </span></td></tr>		<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Non-specific_serine/threonine_protein_kinase Non-specific serine/threonine protein kinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.11.1 2.7.11.1] </span></td></tr>
-	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3r0t FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3r0t OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3r0t RCSB], [http://www.ebi.ac.uk/pdbsum/3r0t PDBsum]</span></td></tr>	+	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3r0t FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3r0t OCA], [http://pdbe.org/3r0t PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3r0t RCSB], [http://www.ebi.ac.uk/pdbsum/3r0t PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3r0t ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
Line 19:		Line 20:
	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>		From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
	</div>		</div>
		+	<div class="pdbe-citations 3r0t" style="background-color:#fffaf0;"></div>

	==See Also==		==See Also==

OCA at 18:09, 25 December 2014

2014-12-25T18:09:42Z

←Older revision		Revision as of 18:09, 25 December 2014
Line 2:		Line 2:
	<StructureSection load='3r0t' size='340' side='right' caption='[[3r0t]], [[Resolution\|resolution]] 1.75Å' scene=''>		<StructureSection load='3r0t' size='340' side='right' caption='[[3r0t]], [[Resolution\|resolution]] 1.75Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[3r0t]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3R0T OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3R0T FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[3r0t]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3R0T OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3R0T FirstGlance]. <br>
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=FU9:3-(CYCLOPROPYLAMINO)-5-{[3-(TRIFLUOROMETHYL)PHENYL]AMINO}PYRIMIDO[4,5-C]QUINOLINE-8-CARBOXYLIC+ACID'>FU9</scene>, <scene name='pdbligand=PEG:DI(HYDROXYETHYL)ETHER'>PEG</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>		</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=FU9:3-(CYCLOPROPYLAMINO)-5-{[3-(TRIFLUOROMETHYL)PHENYL]AMINO}PYRIMIDO[4,5-C]QUINOLINE-8-CARBOXYLIC+ACID'>FU9</scene>, <scene name='pdbligand=PEG:DI(HYDROXYETHYL)ETHER'>PEG</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[3pe1\|3pe1]], [[3pe2\|3pe2]]</td></tr>		<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[3pe1\|3pe1]], [[3pe2\|3pe2]]</td></tr>
		+	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">CSNK2A1, CK2A1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>
	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Non-specific_serine/threonine_protein_kinase Non-specific serine/threonine protein kinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.11.1 2.7.11.1] </span></td></tr>		<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Non-specific_serine/threonine_protein_kinase Non-specific serine/threonine protein kinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.11.1 2.7.11.1] </span></td></tr>
	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3r0t FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3r0t OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3r0t RCSB], [http://www.ebi.ac.uk/pdbsum/3r0t PDBsum]</span></td></tr>		<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3r0t FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3r0t OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3r0t RCSB], [http://www.ebi.ac.uk/pdbsum/3r0t PDBsum]</span></td></tr>
	</table>		</table>
		+	== Function ==
		+	[[http://www.uniprot.org/uniprot/CSK21_HUMAN CSK21_HUMAN]] Catalytic subunit of a constitutively active serine/threonine-protein kinase complex that phosphorylates a large number of substrates containing acidic residues C-terminal to the phosphorylated serine or threonine. Regulates numerous cellular processes, such as cell cycle progression, apoptosis and transcription, as well as viral infection. May act as a regulatory node which integrates and coordinates numerous signals leading to an appropriate cellular response. During mitosis, functions as a component of the p53/TP53-dependent spindle assembly checkpoint (SAC) that maintains cyclin-B-CDK1 activity and G2 arrest in response to spindle damage. Also required for p53/TP53-mediated apoptosis, phosphorylating 'Ser-392' of p53/TP53 following UV irradiation. Can also negatively regulate apoptosis. Phosphorylates the caspases CASP9 and CASP2 and the apoptotic regulator NOL3. Phosphorylation protects CASP9 from cleavage and activation by CASP8, and inhibits the dimerization of CASP2 and activation of CASP8. Regulates transcription by direct phosphorylation of RNA polymerases I, II, III and IV. Also phosphorylates and regulates numerous transcription factors including NF-kappa-B, STAT1, CREB1, IRF1, IRF2, ATF1, SRF, MAX, JUN, FOS, MYC and MYB. Phosphorylates Hsp90 and its co-chaperones FKBP4 and CDC37, which is essential for chaperone function. Regulates Wnt signaling by phosphorylating CTNNB1 and the transcription factor LEF1. Acts as an ectokinase that phosphorylates several extracellular proteins. During viral infection, phosphorylates various proteins involved in the viral life cycles of EBV, HSV, HBV, HCV, HIV, CMV and HPV.<ref>PMID:11239457</ref> <ref>PMID:11704824</ref> <ref>PMID:16193064</ref> <ref>PMID:19188443</ref>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
	== Publication Abstract from PubMed ==		== Publication Abstract from PubMed ==
Line 16:		Line 19:
	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>		From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
	</div>		</div>
		+
		+	==See Also==
		+	*[[Casein kinase\|Casein kinase]]
	== References ==		== References ==
	<references/>		<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
		+	[[Category: Human]]
	[[Category: Non-specific serine/threonine protein kinase]]		[[Category: Non-specific serine/threonine protein kinase]]
-	[[Category: Battistutta, R.]]	+	[[Category: Battistutta, R]]
-	[[Category: Haddach, M.]]	+	[[Category: Haddach, M]]
-	[[Category: Lolli, G.]]	+	[[Category: Lolli, G]]
-	[[Category: Papinutto, E.]]	+	[[Category: Papinutto, E]]
-	[[Category: Pierre, F.]]	+	[[Category: Pierre, F]]
-	[[Category: Ryckman, D M.]]	+	[[Category: Ryckman, D M]]
	[[Category: Ck2-inhibitor complex]]		[[Category: Ck2-inhibitor complex]]
	[[Category: Kinase]]		[[Category: Kinase]]
	[[Category: Transferase-transferase inhibitor complex]]		[[Category: Transferase-transferase inhibitor complex]]

OCA at 09:31, 29 October 2014

2014-10-29T09:31:54Z

←Older revision		Revision as of 09:31, 29 October 2014
Line 2:		Line 2:
	<StructureSection load='3r0t' size='340' side='right' caption='[[3r0t]], [[Resolution\|resolution]] 1.75Å' scene=''>		<StructureSection load='3r0t' size='340' side='right' caption='[[3r0t]], [[Resolution\|resolution]] 1.75Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[3r0t]] is a 1 chain structure ~~with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]~~. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3R0T OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3R0T FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[3r0t]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3R0T OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3R0T FirstGlance]. <br>
-	</td></tr><tr><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=FU9:3-(CYCLOPROPYLAMINO)-5-{[3-(TRIFLUOROMETHYL)PHENYL]AMINO}PYRIMIDO[4,5-C]QUINOLINE-8-CARBOXYLIC+ACID'>FU9</scene>, <scene name='pdbligand=PEG:DI(HYDROXYETHYL)ETHER'>PEG</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene><br>	+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=FU9:3-(CYCLOPROPYLAMINO)-5-{[3-(TRIFLUOROMETHYL)PHENYL]AMINO}PYRIMIDO[4,5-C]QUINOLINE-8-CARBOXYLIC+ACID'>FU9</scene>, <scene name='pdbligand=PEG:DI(HYDROXYETHYL)ETHER'>PEG</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
-	<tr><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[3pe1\|3pe1]], [[3pe2\|3pe2]]</td></tr>	+	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[3pe1\|3pe1]], [[3pe2\|3pe2]]</td></tr>
-	<tr~~><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">CSNK2A1, CK2A1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&~~id=~~9606 Homo sapiens])</td></tr>~~	+	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Non-specific_serine/threonine_protein_kinase Non-specific serine/threonine protein kinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.11.1 2.7.11.1] </span></td></tr>
-	~~<tr~~><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Non-specific_serine/threonine_protein_kinase Non-specific serine/threonine protein kinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.11.1 2.7.11.1] </span></td></tr>	+	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3r0t FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3r0t OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3r0t RCSB], [http://www.ebi.ac.uk/pdbsum/3r0t PDBsum]</span></td></tr>
-	<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3r0t FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3r0t OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3r0t RCSB], [http://www.ebi.ac.uk/pdbsum/3r0t PDBsum]</span></td></tr>	+	</table>
-	<table>	+
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
	== Publication Abstract from PubMed ==		== Publication Abstract from PubMed ==
Line 15:		Line 14:
	Unprecedented selectivity and structural determinants of a new class of protein kinase CK2 inhibitors in clinical stage for the treatment of cancer.,Battistutta R, Cozza G, Pierre F, Papinutto E, Lolli G, Sarno S, O'Brien SE, Siddiqui-Jain A, Haddach M, Anderes K, Ryckman DM, Meggio F, Pinna LA Biochemistry. 2011 Aug 26. PMID:21870818<ref>PMID:21870818</ref>		Unprecedented selectivity and structural determinants of a new class of protein kinase CK2 inhibitors in clinical stage for the treatment of cancer.,Battistutta R, Cozza G, Pierre F, Papinutto E, Lolli G, Sarno S, O'Brien SE, Siddiqui-Jain A, Haddach M, Anderes K, Ryckman DM, Meggio F, Pinna LA Biochemistry. 2011 Aug 26. PMID:21870818<ref>PMID:21870818</ref>

-	From ~~MEDLINEÂ®~~/~~PubMedÂ®~~, a database of the U.S. National Library of Medicine.<br>	+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
	</div>		</div>
-
-	==See Also==
-	*[[Casein kinase\|Casein kinase]]
	== References ==		== References ==
	<references/>		<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: Homo sapiens]]
	[[Category: Non-specific serine/threonine protein kinase]]		[[Category: Non-specific serine/threonine protein kinase]]
	[[Category: Battistutta, R.]]		[[Category: Battistutta, R.]]
-	[[Category: G., Lolli.]]
	[[Category: Haddach, M.]]		[[Category: Haddach, M.]]
		+	[[Category: Lolli, G.]]
	[[Category: Papinutto, E.]]		[[Category: Papinutto, E.]]
	[[Category: Pierre, F.]]		[[Category: Pierre, F.]]

OCA at 04:47, 5 June 2014

2014-06-05T04:47:05Z

←Older revision		Revision as of 04:47, 5 June 2014
Line 1:		Line 1:
-	[[~~Image:~~3r0t.~~jpg~~\|~~left~~\|~~200px~~]]	+	==Crystal structure of human protein kinase CK2 alpha subunit in complex with the inhibitor CX-5279==
		+	<StructureSection load='3r0t' size='340' side='right' caption='[[3r0t]], [[Resolution\|resolution]] 1.75Å' scene=''>
		+	== Structural highlights ==
		+	<table><tr><td colspan='2'>[[3r0t]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3R0T OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3R0T FirstGlance]. <br>
		+	</td></tr><tr><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=FU9:3-(CYCLOPROPYLAMINO)-5-{[3-(TRIFLUOROMETHYL)PHENYL]AMINO}PYRIMIDO[4,5-C]QUINOLINE-8-CARBOXYLIC+ACID'>FU9</scene>, <scene name='pdbligand=PEG:DI(HYDROXYETHYL)ETHER'>PEG</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene><br>
		+	<tr><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[3pe1\|3pe1]], [[3pe2\|3pe2]]</td></tr>
		+	<tr><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">CSNK2A1, CK2A1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens])</td></tr>
		+	<tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Non-specific_serine/threonine_protein_kinase Non-specific serine/threonine protein kinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.11.1 2.7.11.1] </span></td></tr>
		+	<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3r0t FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3r0t OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3r0t RCSB], [http://www.ebi.ac.uk/pdbsum/3r0t PDBsum]</span></td></tr>
		+	<table>
		+	<div style="background-color:#fffaf0;">
		+	== Publication Abstract from PubMed ==
		+	5-(3-chlorophenylamino)benzo[c][2,6] naphthyridine-8 carboxylic acid (CX-4945), the first clinical stage inhibitor of protein kinase CK2 for the treatment of cancer, is representative of a new class of CK2 inhibitors with Ki values in the low nanomolar range and unprecedented selectivity versus other kinases. Here we present the crystal structure of the complexes between CX-4945 and two analogs (CX-5011 and CX-5279) with the catalytic subunit of human CK2. Consistent with their ATP competitive mode of inhibition, all three compounds bind in the active site of CK2 (Type I inhibitors). The tricyclic scaffold of the inhibitors superposes to the adenine of ATP establishing multiple hydrophobic interactions with the binding cavity. The more extended scaffold, as compared to that of ATP, allows the carboxylic function, shared by all three ligands, to penetrate into the deepest part of the active site where it makes interactions with conserved water W1 and Lys-68, thus accounting for the crucial role of this negatively charged group in conferring high potency to this class of inhibitors. The presence of a pyrimidine in CX-5011 and in CX-5279 instead of a pyridine (as in CX-4945) ring is likely to account for the higher specificity of these compounds whose Gini coefficients, calculated by profiling them against panels of 102 and/or 235 kinases, are significantly higher than that of CX-4945 (0.735 and 0.755 respectively, vs 0.615), denoting the highest selectivity ever reported for CK2 inhibitors.

-	~~<!-~~-	+	Unprecedented selectivity and structural determinants of a new class of protein kinase CK2 inhibitors in clinical stage for the treatment of cancer.,Battistutta R, Cozza G, Pierre F, Papinutto E, Lolli G, Sarno S, O'Brien SE, Siddiqui-Jain A, Haddach M, Anderes K, Ryckman DM, Meggio F, Pinna LA Biochemistry. 2011 Aug 26. PMID:21870818<ref>PMID:21870818</ref>
-	~~The line below this paragraph~~, ~~containing "STRUCTURE_3r0t"~~, ~~creates the "Structure Box" on the page.~~	+
-	~~You may change the PDB parameter (which sets the PDB file loaded into the applet)~~	+
-	~~or the SCENE parameter (which sets the initial scene displayed when the page is loaded)~~,	+
-	~~or leave the SCENE parameter empty for the default display~~.	+
-	-->	+
-	~~{{STRUCTURE_3r0t\| PDB=3r0t \| SCENE= }}~~	+

-	~~===Crystal structure~~ of ~~human protein kinase CK2 alpha subunit in complex with~~ the ~~inhibitor CX-5279===~~	+	From MEDLINEÂ®/PubMedÂ®, a database of the U.S. National Library of Medicine.<br>
		+	</div>

-		+	==See Also==
-	~~<!--~~	+	*[[Casein kinase\|Casein kinase]]
-	~~The line below this paragraph, {{ABSTRACT_PUBMED_21870818}}, adds the Publication Abstract to the page~~	+	== References ==
-	~~(as it appears on PubMed at http://www.pubmed.gov), where 21870818 is the PubMed ID number.~~	+	<references/>
-	~~-->~~	+	__TOC__
-	~~{{ABSTRACT_PUBMED_21870818}}~~	+	</StructureSection>
-		+
-	==~~About this Structure~~==	+
-	[[~~3r0t~~]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3R0T OCA].	+
-		+
-	==~~Reference~~==	+
-	<~~ref group="xtra">PMID:021870818<~~/~~ref~~><~~ref group="xtra">PMID:019432557</ref><references group="xtra"~~/>	+
	[[Category: Homo sapiens]]		[[Category: Homo sapiens]]
	[[Category: Non-specific serine/threonine protein kinase]]		[[Category: Non-specific serine/threonine protein kinase]]

OCA at 08:06, 7 December 2011

2011-12-07T08:06:30Z

←Older revision		Revision as of 08:06, 7 December 2011
Line 1:		Line 1:
-	~~'''Unreleased structure'''~~	+	[[Image:3r0t.jpg\|left\|200px]]

-	The ~~entry 3r0t~~ is ~~ON HOLD~~ ~~until Paper Publication~~	+	<!--
		+	The line below this paragraph, containing "STRUCTURE_3r0t", creates the "Structure Box" on the page.
		+	You may change the PDB parameter (which sets the PDB file loaded into the applet)
		+	or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
		+	or leave the SCENE parameter empty for the default display.
		+	-->
		+	{{STRUCTURE_3r0t\| PDB=3r0t \| SCENE= }}

-	~~Authors: Battistutta, R., Papinutto, E., Lolli G., Pierre, F., Haddach, M., Ryckman, D.M.~~	+	===Crystal structure of human protein kinase CK2 alpha subunit in complex with the inhibitor CX-5279===

-	~~Description~~: ~~Crystal~~ structure ~~of human~~ protein kinase ~~CK2 alpha subunit in complex with the~~ inhibitor CX-~~5279~~	+
		+	<!--
		+	The line below this paragraph, {{ABSTRACT_PUBMED_21870818}}, adds the Publication Abstract to the page
		+	(as it appears on PubMed at http://www.pubmed.gov), where 21870818 is the PubMed ID number.
		+	-->
		+	{{ABSTRACT_PUBMED_21870818}}
		+
		+	==About this Structure==
		+	[[3r0t]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3R0T OCA].
		+
		+	==Reference==
		+	<ref group="xtra">PMID:021870818</ref><ref group="xtra">PMID:019432557</ref><references group="xtra"/>
		+	[[Category: Homo sapiens]]
		+	[[Category: Non-specific serine/threonine protein kinase]]
		+	[[Category: Battistutta, R.]]
		+	[[Category: G., Lolli.]]
		+	[[Category: Haddach, M.]]
		+	[[Category: Papinutto, E.]]
		+	[[Category: Pierre, F.]]
		+	[[Category: Ryckman, D M.]]
		+	[[Category: Ck2-inhibitor complex]]
		+	[[Category: Kinase]]
		+	[[Category: Transferase-transferase inhibitor complex]]

OCA at 04:56, 13 April 2011

2011-04-13T04:56:34Z

←Older revision		Revision as of 04:56, 13 April 2011
Line 1:		Line 1:
	'''Unreleased structure'''		'''Unreleased structure'''

-	The entry 3r0t is ON HOLD	+	The entry 3r0t is ON HOLD until Paper Publication

	Authors: Battistutta, R., Papinutto, E., Lolli G., Pierre, F., Haddach, M., Ryckman, D.M.		Authors: Battistutta, R., Papinutto, E., Lolli G., Pierre, F., Haddach, M., Ryckman, D.M.

	Description: Crystal structure of human protein kinase CK2 alpha subunit in complex with the inhibitor CX-5279		Description: Crystal structure of human protein kinase CK2 alpha subunit in complex with the inhibitor CX-5279

OCA: Protected "3r0t" [edit=sysop:move=sysop]

2011-03-16T08:07:26Z

Protected "3r0t" [edit=sysop:move=sysop]

←Older revision

Revision as of 08:07, 16 March 2011

OCA: New page: '''Unreleased structure''' The entry 3r0t is ON HOLD Authors: Battistutta, R., Papinutto, E., Lolli G., Pierre, F., Haddach, M., Ryckman, D.M. Description: Crystal structure of human p...

2011-03-16T08:07:25Z

New page: '''Unreleased structure''' The entry 3r0t is ON HOLD Authors: Battistutta, R., Papinutto, E., Lolli G., Pierre, F., Haddach, M., Ryckman, D.M. Description: Crystal structure of human p...

New page

'''Unreleased structure'''

The entry 3r0t is ON HOLD

Authors: Battistutta, R., Papinutto, E., Lolli G., Pierre, F., Haddach, M., Ryckman, D.M.

Description: Crystal structure of human protein kinase CK2 alpha subunit in complex with the inhibitor CX-5279